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At least 397 records · Page 22Linked to original sources
PubMed2005

Polyphenol oxidase from Dominga table grape.

Dominga grape polyphenol oxidase (PPO) was extracted using phase partitioning with Triton X-114. The enzyme was obtained in latent state and could be optimally activated by the presence of 0.2% sodium dodecyl sulfate (SDS) at pH 6.0. In the absence of SDS, the enzyme showed maximum activity at acid pH. The kinetic parameters of the enzyme at pH 3.0 and 6.0 in the presence of SDS were calculated. The effect of several inhibitors was studied, tropolone being the most effective with a K(i) value of 18 muM. The effect of cyclodextrins was also studied, and the complexation constant K(c) between G(2)-beta-cyclodextrins and 4-tert-butylcatechol was calculated using the enzymatic method (K(c) = 13960 M(-)(1)). The evolution of the color parameters (L, a, b) of liquefied grape berries was inhibited by inhibitors of PPO activity, such as diethyldithiocarbamate, metabisulfite, and G(2)-beta-cyclodextrins, indicating that enzymatic browning by PPO is the main process involved in the browning of Dominga grape juice at room temperature.

Catechol Oxidase↗
PubMed1999

Characterization of tyrosinase from the cap flesh of portabella mushrooms.

Tyrosinase, purified from the cap flesh tissue of portabella mushrooms, was characterized with regard to its physical and biochemical properties. A native molecular size of 41 kDa for the enzyme was obtained by size exclusion chromatography, whereas SDS-PAGE indicated that the enzyme contained a single subunit with a size of approximately 48 kDa under reduced and nonreduced conditions. The purified enzyme showed a single immunological cross-reacting protein after Western blotting when probed with antibodies against Agaricus bisporus tyrosinase. Isoelectric focusing demonstrated that the enzyme preparation, apparently homogeneous by electrophoresis, still contained three isoforms of pI 5.1, 5.2, and 5.3. The purified enzyme was able to oxidize a variety of mono-, di-, and triphenolic compounds. An apparent K(m) of 5 mM was obtained using catechol as the substrate, and an apparent K(m) of 9 mM was found using L-Dopa as a substrate. Ascorbic acid, kojic acid, tropolone, mercaptobenzothiazole, and salicylhydroxamic acid inhibited the enzyme severely at 100 microM.

Agaricus↗
PubMed2000

Characterization of catecholase and cresolase activities of eggplant polyphenol oxidase.

In the present paper the catecholase and cresolase activities of eggplant polyphenol oxidase (PPO) are described. To preserve the latter activity, a partially purified enzyme was used. Peroxidase was removed from the preparation to avoid its interference with PPO during phenol oxidation. The partially purified eggplant PPO was fully active. The catecholase/cresolase ratio of 41.1 indicated that, in a pH close to the physiological, diphenol oxidation predominates over monophenol oxidation. The characteristic lag phase of the cresolase activity is modulated by the pH, the monophenol and diphenol concentrations, and the enzyme's concentration. The effect of several inhibitors was also tested, and the K(i) values of the two most effective (tropolone and 4-hexylresorcinol) were determined.

Catechol Oxidase↗
PubMed1981

Quantitative structure-activity relationships of colchicines against P388 leukemia in mice.

A quantitative structure-activity relationship (QSAR) was derived for colchicine and 14 analogues acting against P388 lymphocytic leukemia in mice. Twelve additional compounds were synthesized to reinforce and confirm the correlation. The final correlation indicates that there is a parabolic dependence of antitumor potency on the partition coefficient with log P0=1.17. When an amino nitrogen is present on the B ring, increased potency is favored by acylation of the nitrogen. The most potent compound of the series was the 7-fluoroacetamide analogue. Strong electron-withdrawing groups substituted at the 10 position of the tropolone ring destroy activity. Electron-releasing groups at position 10 improve potency slightly but have a limited effect.

Animals↗
PubMed1981

Biological effects of modified colchicines. Improved preparation of 2-demethylcolchicine, 3-demethylcolchicine, and (+)-colchicine and reassignment of the position of the double bond in dehydro-7-deacetamidocolchicines.

A variety of colchicine, demecolcine, and isocolchicine derivatives were examined for their potency in the lymphocytic leukemia P388 screen in mice, for their toxicity in mice, and for their binding to microtubule protein. A qualitatively direct correlation was found between in vivo potency and toxicity; potency appeared to be less well correlated with tubulin binding. The most potent compounds were N-acylated analogues of colchicine and demecolcine. Among the monophenols, only 3-demethylcolchicine showed an appreciable effect in vitro and in vivo and was less toxic than colchicine. Improved methods were found for the preparation of 3- and 2-demethylcolchicine, which involved the use of 85% phosphoric acid and concentrated sulfuric acid, respectively. Decoupling experiments with 1H NMR proved that the double bond of dehydro-7-deacetamidocolchiceine and its derived tropolonic methyl ethers 24 and 25 was in the 5,6 position, rather than the 6,7 position formerly tentatively assigned.

Animals↗
PubMed2005

Total synthesis of (-)-colchicine via a Rh-triggered cycloaddition cascade.

[reaction: see text] A synthesis of the antimitotic alkaloids (-)-colchicine and (-)-isocolchicine is reported. Important steps are (a) enantioselective transfer-hydrogenation of an alkynone, (b) iodine/magnesium exchange with subsequent aromatic acylation, (c) Rh-catalyzed transformation of an alpha-diazoketone into an oxatetracyclic key intermediate through intramolecular [3 + 2]-cycloaddition of an in situ generated carbonyl ylide, and (d) regioselective conversion of the cycloadduct into a tropolone derivative. The new synthetic strategy opens an efficient enantioselective access to colchicine and structural analogues.

Colchicine↗
PubMed2003

Seasonal and spatial variations of alkaloids in Merendera montana in relation to chemical defense and phenology.

Merendera montana (Liliaceae) is an endemic plant broadly, but exclusively, occurring in the Iberian Peninsula where it is one of the most abundant species in rangelands grazed by sheep and on the routes used by migrating sheep herds. In spite of showing a peculiar phenology adapted to Mediterranean regions (leaves remain green from fall to spring and are absent in summer), this species has also successfully colonized high altitude environments (up to 2300 m), and abundant populations can be found in montane and subalpine pasturcs. Chemical analysis has shown a high forage quality as well as the presence of tropolone alkaloids (similar to other species of the genus Merendera), mainly colchicine, 3-demethylcolchicine, and colchicoside. In general terms, the alkaloid content was significantly lower in the subterranean corms than in the leaves. No remarkable seasonal variations in total alkaloids was found, although an increase of colchicoside in the corms and a decrease of colchicine was noted in summer. Both chemical deterrents and phenology could be the cause of the widespread ecological adaptation of Merendera montana. The alkaloid content would prevent intake by wild herbivores during winter, while the absence of aerial organs in summer, coinciding exactly with the highest domestic herbivore pressure, would permit this species to colonize rich soil habitats where there is low plant competition.

Adaptation, Physiological↗
PubMed1992

Effect of the deposition potential on the voltammetric determination of complexing ligand concentrations in sea-water.

The effect of the deposition potential on the determination of complexing ligand concentrations in natural waters was investigated by titration with Cu from sea-water samples originating from the North Sea and monitoring the labile Cu concentration after deposition at two potentials, viz., -0.05 and -0.7 V. The amount of deposited metal was measured by cathodic stripping voltammetry with ligand competition, using tropolone as the added ligand. It was found that the complexing ligand concentration detected decreased by more than 60% when the more negative deposition potential was applied. The data indicate that a significant fraction of the organic complexes of Cu in natural waters is electrochemically labile at negative deposition potentials and is not determined by anodic stripping voltammetry. The concentrations and conditional stability constants of the complexing ligands in the North Sea are similar to those detected previously in the Irish Sea.

Copper↗
PubMed1992

Determination of butyltin species in sewage and sludge by gas chromatography-atomic absorption spectrometry.

A method for the extraction and determination of butyltin compounds in sewage and sludge is reported. Sewage and sludge samples are acidified and shaken for 2 h. The various butyltin species are extracted quantitatively by tropolone (cycloheptatrienone) in toluene, followed by ethylation to their tetraalkyl-substituted forms, BuSnEt3, Bu2SnEt2, Bu3SnEt and Et4Sn, all of which can be separated and determined by a gas chromatographic-atomic absorption spectrometric technique. The non-pesticidal octyltin species and acid-leachable SnIV species can also be determined by this method. Detection limits expressed as Sn are 40 ng dm-3 and 2 ng g-1 dry mass for sewage and sludge, respectively. Analyses of some samples from Canadian treatment plants are given.

Chromatography, Gas↗
PubMed2000

A quantitative extraction method for the determination of trace amounts of both butyl- and phenyltin compounds in sediments by gas chromatography-inductively coupled plasma mass spectrometry.

A simple and reliable extraction method was developed for quantitative determination of both butyl- and phenyltin compounds in sediments by capillary gas chromatography combined with inductively coupled plasma mass spectrometry (GC-ICP-MS). Both types of organotin compounds were extracted quantitatively from sediment by mechanical shaking into tropolone-toluene and HCl-methanol. After phase separation and pH adjustment, these organotins were ethylated with sodium tetraethylborate. The method was evaluated by analyzing PACS-2 and NIES No. 12 sediment certified reference materials. The dibutyltin (DBT; 1.14 +/- 0.02 micrograms g-1) and tributyltin (TBT; 1.01 +/- 0.04 micrograms g-1) values observed in PACS-2 sediment closely matched the certified values (DBT, 1.09 +/- 0.15; TBT, 0.98 +/- 0.13 microgram g-1 as tin). The monobutyltin (MBT) value was higher (0.62 +/- 0.02 microgram g-1) by more than two fold over the reference value (0.3 microgram g-1 as tin). The concentrations of TBT (0.18 +/- 0.04 microgram g-1) and triphenyltin (TPhT; 0.0099 +/- 0.002 microgram g-1) in the NIES No. 12 sediment were also in good agreement with the certified and reference values of TBT (0.19 +/- 0.03 microgram g-1 as compound) and TPhT (0.008 microgram g-1 as compound), respectively. Recoveries of TBT, tripentyltin (TPeT) and TPhT from spiked sediments were satisfactory (TBT, 102 +/- 3.4%; TPrT, 96 +/- 3.4%; TPhT, 99 +/- 8.5%). The detection limits as tin were in the range 0.23-0.48 ng g-1 for a 0.5 g sample size. It is also noteworthy that clean-up of the extract is not necessary because of the superior selectivity of ICP-MS detection. The present method was successfully applied to marine sediment samples.

Environmental Pollutants↗
PubMed2003

Tautomeric selectivity towards colchicinoids in the tosylation of colchiceine on a heterogeneous, easily removable catalyst.

Here is presented an easy, rapid new method of tosylation of compounds containing acidic OH groups, such as tropolones and phenols, on a solid, removable catalyst, Amberlite IRA-400(OH); of special value is the preferential selectivity for the colchiceine tautomer 1a, leading to 10-tosyloxycolchicide (2)--the precursor of a variety of bioactive colchicinoids--which inverts the result of previous tosylation methodologies leading preferentially to useless 9-tosyloxyisocolchicide (3).

Catalysis↗
PubMed2005

Rhodium hydride formation in the presence of a bulky monophosphite ligand: a spectroscopic and solid-state investigation.

A study has been carried out on rhodium catalyst preforming when modified with the bulky tris(2,4-di-tert-butylphenyl) phosphite, P(Obtbp)(3). X-Ray crystal structure determinations of a tropolone-type precursor complex [Rh(TropBr(3))(CO){P(Obtbp)(3)}].P(Obtbp)(3).CH(3)COCH(3)(TropBr(3)= 3,5,7-tribromotropolonate) and the free P(Obtbp)(3) ligand are reported. Systematic in situ IR and NMR studies of the particular rhodium phosphite modified catalyst and its precursors have led to the identification of two distinct rhodium hydride species. A {(1)H,(31)P} HMBC NMR experiment afforded clarity on the (31)P NMR spectra observed under hydroformylation conditions. The species were identified as [HRh(CO)(3){P(Obtbp)(3)}] and [HRh(CO)(2){P(Obtbp)(3)}(2)]. Attention was also given to the rate of catalyst formation when starting from different rhodium precursors.

Journal Article↗
PubMed2005

The influence of ligand field effects on the magnetic exchange of high-spin Co(II)-semiquinonate complexes.

[Co(Me(4)cyclam)(tropolonate)](PF(6)) was synthesised and structurally characterised. Its electronic and W-band EPR spectra have been analysed by means of the angular overlap calculation of the Spin Hamiltonian parameters that provided also a satisfactory reproduction of the temperature dependence of the magnetic susceptibility. The present results can be interpreted assuming a pseudo-octahedral character for the Co(II) center. This prompted us to reconsider the model formerly used for the analysis of the magnetic coupling between hs-Co(II) and the paramagnetic o-semiquinonate ligand in the corresponding derivatives [Co(Me(4)cyclam)(PhenSQ)](PF(6)) and [Co(Me(4)cyclam)(DTBSQ)](PF(6)). These results indicate that the effect of the magnetic coupling is active only below 50 K and that a more refined model of exchange coupling between Co(II) and semiquinonato ligands is needed to quantitatively analyze the magnetic behaviour of this class of systems.

Journal Article↗
PubMed2004

Shear-stress preconditioning and tissue-engineering-based paradigms for generating arterial substitutes.

In situ tissue engineering using shear-stress preconditioning and adhesive biomolecules is a new approach to autologous tissue engineering. In the present study, novel tissue-engineering grafts (TEGs) were preconditioned within an in vitro pulsatile flow circuit, with and without the addition of fibronectin (FN), to establish whether low-shear-stress conditions promoted endothelial cell (EC) retention and differentiation. TEGs ( n =24) were generated by the contraction and compaction of collagen(I) by porcine aortic smooth-muscle cells (SMCs) on to a compliant polyester graft scaffold. ECs were radiolabelled with [(111)In]indium tropolonate and seeded on to the luminal surface of the TEGs. Following organ culture in a bioreactor (7 days), TEGs were split into four groups ( n =six TEGs per group): Group A acted as controls with TEGs unmodified and seeded with radiolabelled ECs; Group B underwent luminal pre-coating with FN (75 microg/ml) prior to EC seeding; Group C underwent preconditioning within a pulsatile flow circuit at 10-20 microN (1-2 dyn)/cm(2) for 7 days prior to EC seeding, and Group D TEGs were preconditioned for 7 days at 1-2 dyn/cm(2), followed by luminal pre-coating with FN prior to EC seeding. The resistance to physiological shear stress of the seeded ECs was assessed using a gamma-radiation counter within a physiological flow circuit producing an arterial waveform with a mean shear stress of 93.2 microN (9.32 dyn)/cm(2). Environmental scanning electron microscopy (ESEM) was used to determine the distribution and degree of differentiation of the attached Ecs, and tissue-type-plasminogen-activator (tPA) assays provided a measure of function and viability. EC resistance to shear stress at 93.2 microN/cm(2) was significantly enhanced by a period of preconditioning (Group C) at 10-20 microN/cm(2), surface modification with FN (Group B), or both (Group D) when compared with control grafts (Group A). However, TEGs coated with FN whether preconditioned (Group D) or not (Group B) demonstrated the best results for EC retention. ESEM demonstrated near-confluent differentiated flattened ECs in both these cases. EC function was demonstrated by a steady increase in tPA production. Low-shear-stress preconditioning of TEGs enhances EC retention in vitro with an additional advantage demonstrated by pre-treatment with FN prior to endothelialization. These findings may be exploited in the development of tissue-engineered constructs to maintain a confluent endothelial lining.

Adaptation, Physiological↗
PubMed2006

The conformational state of polyphenol oxidase from field bean (Dolichos lablab) upon SDS and acid-pH activation.

Field bean (Dolichos lablab) contains a single isoform of PPO (polyphenol oxidase)--a type III copper protein that catalyses the o-hydroxylation of monophenols and oxidation of o-diphenols using molecular oxygen--and is a homotetramer with a molecular mass of 120 kDa. The enzyme is activated manyfold either in the presence of the anionic detergent SDS below its critical micellar concentration or on exposure to acid-pH. The enhancement of kcat upon activation is accompanied by a marked shift in the pH optimum for the oxidation of t-butyl catechol from 4.5 to 6.0, an increased sensitivity to tropolone, altered susceptibility to proteolytic degradation and decreased thermostability. The Stokes radius of the native enzyme is found to increase from 49.1+/-2 to 75.9+/-0.6 A (1 A=0.1 nm). The activation by SDS and acid-pH results in a localized conformational change that is anchored around the catalytic site of PPO that alters the microenvironment of an essential glutamic residue. Chemical modification of field bean and sweet potato PPO with 1-ethyl-3-(3-dimethylaminopropyl)carbodi-imide followed by kinetic analysis leads to the conclusion that both the enzymes possess a core carboxylate essential to activity. This enhanced catalytic efficiency of PPO, considered as an inducible defence oxidative enzyme, is vital to the physiological defence strategy adapted by plants to insect herbivory and pathogen attack.

Acids↗
PubMed1991

Specificity of dopachrome tautomerase and inhibition by carboxylated indoles. Considerations on the enzyme active site.

Dopachrome tautomerase (EC 5.3.2.3) catalyses the tautomerization of dopachrome to 5,6-dihydroxyindole-2-carboxylic acid (DHICA) within the melanin-formation pathway. We have analysed a series of substrate analogues and related compounds as possible substrates and inhibitors of tautomerization. The enzyme appears to be highly specific since D-dopachrome, alpha-methyldopachrome, dopaminochrome, adrenochrome methyl ether and deoxyadrenochrome are not substrates. Conversely, dopachrome tautomerase catalyses the tautomerization of dopachrome methyl ester, suggesting that a carboxy group, either free or as a methyl ester, is essential for enzyme recognition. No inhibition of dopachrome tautomerization was observed in the presence of either semiquinonic compounds, such as tropolone and L-mimosine, or pyrrole-2-carboxylic acid and unsubstituted indole. However, a number of indole derivatives, including DHICA, the product of dopachrome tautomerization, and the analogues 5-hydroxyindole-2-carboxylic and indole-2-carboxylic acid were able to inhibit the enzyme. Furthermore, indoles with a side chain at position 3 of the ring and containing a carboxylic group at the gamma-position of this chain, such as L-tryptophan or indole-3-propionic acid, are stronger inhibitors of the enzyme. Indole-3-carboxylic acid, indole-3-acetic acid and indole-3-butyric acid are very weak inhibitors, showing that the carboxylic group needs to be located at an optimal distance from the indole ring to mimic the carboxylic group at position 2 on the authentic substrate.

Ammonium Sulfate↗
PubMed1994

A new dopachrome-rearranging enzyme from the ejected ink of the cuttlefish Sepia officinalis.

A melanogenic enzyme catalysing the rearrangement of dopachrome has been identified in the ejected ink of the cuttlefish Sepia officinalis. This enzyme occurs as a heat-labile protein which co-migrates with tyrosinase under a variety of chromatographic and electrophoretic conditions. On SDS/PAGE it shows like a single band with an approx. molecular mass of 85 kDa. The enzyme possesses high substrate specificity, acting on L-dopachrome (Km = 1 mM at pH 6.8) and on L-alpha-methyl-dopachrome, but not on D-dopachrome, L-dopachrome methyl ester, dopaminochrome and adrenochrome. Significant inhibition of the catalytic activity was observed with tropolone and L-mimosine. H.p.1.c. analysis of the enzyme-catalysed rearrangement of L-dopachrome revealed the quantitative formation of the decarboxylated product, 5,6-dihydroxyindole. These results point to marked differences between melanogenesis in cephalopod pigment cells and in melanocytes, which may have important implications in relation to the use of sepiomelanin as a model for studies of mammalian melanins.

Animals↗